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Database: UniProt
Entry: H2ZL34_CIOSA
LinkDB: H2ZL34_CIOSA
Original site: H2ZL34_CIOSA 
ID   H2ZL34_CIOSA            Unreviewed;      1478 AA.
AC   H2ZL34;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   24-JAN-2024, entry version 64.
DE   RecName: Full=NAD(P)H oxidase (H2O2-forming) {ECO:0000256|ARBA:ARBA00012698};
DE            EC=1.6.3.1 {ECO:0000256|ARBA:ARBA00012698};
OS   Ciona savignyi (Pacific transparent sea squirt).
OC   Eukaryota; Metazoa; Chordata; Tunicata; Ascidiacea; Phlebobranchia;
OC   Cionidae; Ciona.
OX   NCBI_TaxID=51511 {ECO:0000313|Ensembl:ENSCSAVP00000018300.1, ECO:0000313|Proteomes:UP000007875};
RN   [1] {ECO:0000313|Proteomes:UP000007875}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Birren B., Nusbaum C., Abebe A., Abouelleil A., Adekoya E., Ait-zahra M.,
RA   Allen N., Allen T., An P., Anderson M., Anderson S., Arachchi H.,
RA   Armbruster J., Bachantsang P., Baldwin J., Barry A., Bayul T.,
RA   Blitshsteyn B., Bloom T., Blye J., Boguslavskiy L., Borowsky M.,
RA   Boukhgalter B., Brunache A., Butler J., Calixte N., Calvo S., Camarata J.,
RA   Campo K., Chang J., Cheshatsang Y., Citroen M., Collymore A., Considine T.,
RA   Cook A., Cooke P., Corum B., Cuomo C., David R., Dawoe T., Degray S.,
RA   Dodge S., Dooley K., Dorje P., Dorjee K., Dorris L., Duffey N., Dupes A.,
RA   Elkins T., Engels R., Erickson J., Farina A., Faro S., Ferreira P.,
RA   Fischer H., Fitzgerald M., Foley K., Gage D., Galagan J., Gearin G.,
RA   Gnerre S., Gnirke A., Goyette A., Graham J., Grandbois E., Gyaltsen K.,
RA   Hafez N., Hagopian D., Hagos B., Hall J., Hatcher B., Heller A.,
RA   Higgins H., Honan T., Horn A., Houde N., Hughes L., Hulme W., Husby E.,
RA   Iliev I., Jaffe D., Jones C., Kamal M., Kamat A., Kamvysselis M.,
RA   Karlsson E., Kells C., Kieu A., Kisner P., Kodira C., Kulbokas E.,
RA   Labutti K., Lama D., Landers T., Leger J., Levine S., Lewis D., Lewis T.,
RA   Lindblad-toh K., Liu X., Lokyitsang T., Lokyitsang Y., Lucien O., Lui A.,
RA   Ma L.J., Mabbitt R., Macdonald J., Maclean C., Major J., Manning J.,
RA   Marabella R., Maru K., Matthews C., Mauceli E., Mccarthy M., Mcdonough S.,
RA   Mcghee T., Meldrim J., Meneus L., Mesirov J., Mihalev A., Mihova T.,
RA   Mikkelsen T., Mlenga V., Moru K., Mozes J., Mulrain L., Munson G.,
RA   Naylor J., Newes C., Nguyen C., Nguyen N., Nguyen T., Nicol R., Nielsen C.,
RA   Nizzari M., Norbu C., Norbu N., O'donnell P., Okoawo O., O'leary S.,
RA   Omotosho B., O'neill K., Osman S., Parker S., Perrin D., Phunkhang P.,
RA   Piqani B., Purcell S., Rachupka T., Ramasamy U., Rameau R., Ray V.,
RA   Raymond C., Retta R., Richardson S., Rise C., Rodriguez J., Rogers J.,
RA   Rogov P., Rutman M., Schupbach R., Seaman C., Settipalli S., Sharpe T.,
RA   Sheridan J., Sherpa N., Shi J., Smirnov S., Smith C., Sougnez C.,
RA   Spencer B., Stalker J., Stange-thomann N., Stavropoulos S., Stetson K.,
RA   Stone C., Stone S., Stubbs M., Talamas J., Tchuinga P., Tenzing P.,
RA   Tesfaye S., Theodore J., Thoulutsang Y., Topham K., Towey S., Tsamla T.,
RA   Tsomo N., Vallee D., Vassiliev H., Venkataraman V., Vinson J., Vo A.,
RA   Wade C., Wang S., Wangchuk T., Wangdi T., Whittaker C., Wilkinson J.,
RA   Wu Y., Wyman D., Yadav S., Yang S., Yang X., Yeager S., Yee E., Young G.,
RA   Zainoun J., Zembeck L., Zimmer A., Zody M., Lander E.;
RL   Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSCSAVP00000018300.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JUL-2023) to UniProtKB.
CC   -!- FUNCTION: Generates hydrogen peroxide which is required for the
CC       activity of thyroid peroxidase/TPO and lactoperoxidase/LPO. Plays a
CC       role in thyroid hormones synthesis and lactoperoxidase-mediated
CC       antimicrobial defense at the surface of mucosa. May have its own
CC       peroxidase activity through its N-terminal peroxidase-like domain.
CC       {ECO:0000256|ARBA:ARBA00003796}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + NADH + O2 = H2O2 + NAD(+); Xref=Rhea:RHEA:11264,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.6.3.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00000518};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + NADPH + O2 = H2O2 + NADP(+); Xref=Rhea:RHEA:11260,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.6.3.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00000547};
CC   -!- PATHWAY: Hormone biosynthesis; thyroid hormone biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00005197}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC       Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the peroxidase
CC       family. {ECO:0000256|ARBA:ARBA00005644}.
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DR   Ensembl; ENSCSAVT00000018500.1; ENSCSAVP00000018300.1; ENSCSAVG00000010749.1.
DR   GeneTree; ENSGT00940000163963; -.
DR   HOGENOM; CLU_004482_1_0_1; -.
DR   UniPathway; UPA00194; -.
DR   Proteomes; UP000007875; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0016174; F:NAD(P)H oxidase H2O2-forming activity; IEA:UniProtKB-EC.
DR   GO; GO:0004601; F:peroxidase activity; IEA:InterPro.
DR   GO; GO:0042446; P:hormone biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR   GO; GO:0006590; P:thyroid hormone generation; IEA:UniProtKB-UniPathway.
DR   CDD; cd00051; EFh; 1.
DR   CDD; cd06186; NOX_Duox_like_FAD_NADP; 1.
DR   Gene3D; 1.10.238.10; EF-hand; 1.
DR   Gene3D; 1.10.640.10; Haem peroxidase domain superfamily, animal type; 1.
DR   Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR   Gene3D; 2.40.30.10; Translation factors; 1.
DR   InterPro; IPR011992; EF-hand-dom_pair.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR002048; EF_hand_dom.
DR   InterPro; IPR013112; FAD-bd_8.
DR   InterPro; IPR017927; FAD-bd_FR_type.
DR   InterPro; IPR013130; Fe3_Rdtase_TM_dom.
DR   InterPro; IPR013121; Fe_red_NAD-bd_6.
DR   InterPro; IPR039261; FNR_nucleotide-bd.
DR   InterPro; IPR019791; Haem_peroxidase_animal.
DR   InterPro; IPR010255; Haem_peroxidase_sf.
DR   InterPro; IPR037120; Haem_peroxidase_sf_animal.
DR   InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR   PANTHER; PTHR11972:SF175; DUAL OXIDASE; 1.
DR   PANTHER; PTHR11972; NADPH OXIDASE; 1.
DR   Pfam; PF03098; An_peroxidase; 1.
DR   Pfam; PF13202; EF-hand_5; 2.
DR   Pfam; PF08022; FAD_binding_8; 1.
DR   Pfam; PF01794; Ferric_reduct; 1.
DR   Pfam; PF08030; NAD_binding_6; 1.
DR   PRINTS; PR00457; ANPEROXIDASE.
DR   SFLD; SFLDS00052; Ferric_Reductase_Domain; 1.
DR   SFLD; SFLDG01168; Ferric_reductase_subgroup_(FRE; 1.
DR   SFLD; SFLDG01169; NADPH_oxidase_subgroup_(NOX); 1.
DR   SMART; SM00054; EFh; 2.
DR   SUPFAM; SSF47473; EF-hand; 1.
DR   SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR   SUPFAM; SSF48113; Heme-dependent peroxidases; 1.
DR   SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR   PROSITE; PS00018; EF_HAND_1; 1.
DR   PROSITE; PS50222; EF_HAND_2; 2.
DR   PROSITE; PS51384; FAD_FR; 1.
DR   PROSITE; PS50292; PEROXIDASE_3; 1.
PE   3: Inferred from homology;
KW   Calcium {ECO:0000256|ARBA:ARBA00022837};
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Heme {ECO:0000256|PIRSR:PIRSR619791-2};
KW   Hydrogen peroxide {ECO:0000256|ARBA:ARBA00023324};
KW   Iron {ECO:0000256|PIRSR:PIRSR619791-2};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR619791-2};
KW   NADP {ECO:0000256|ARBA:ARBA00022857};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Peroxidase {ECO:0000256|ARBA:ARBA00023324};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007875};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Thyroid hormones biosynthesis {ECO:0000256|ARBA:ARBA00022534};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        582..605
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        973..995
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1015..1039
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1059..1083
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1103..1132
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1152..1171
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          804..839
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
FT   DOMAIN          840..875
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
FT   DOMAIN          1196..1303
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
FT   BINDING         308
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR619791-2"
SQ   SEQUENCE   1478 AA;  168149 MW;  FC25587C9D0F60A3 CRC64;
     LISKEYPPFN GWYNNRANPA LGVPDSSITR RLPAHYSDGV FLPSGLERPN VRSISNTIMA
     GPSGLPSQNN KTALFLYFGE HVMQDILDTT RPGCPPEYFN VQLNNDATFD VSEMPYERSR
     YQTSNSGYSP NHPREQVNEV TSYLDGSQIY GHTKACLTLI YNKIDGGLEL ASLNDLGEFP
     ALNDIGLPLD NSFTTKDNVI GSGKRFYRLG ARNGNENPFV LTIGVTWFRH HNWLAHVIRD
     LHPDWTDDDV FNEARIENIA TYQSIVLYEW LPILLGTCTP TNSTKCYSSS ASVGISDIFE
     GTARHYLHTL TPPGVFARGT TGSCTFRNIT SALNGGSTTP ALRLCNSFWD PAETFKLISV
     EELTMGMASQ IAELEDNIIT EDLRNHFYGT REFSRRDFVA ILLQKGRDHG LPDYNVARED
     FGLNLKSTFN DINNALFQSN MQDNGTLLRD LEALHTGDLS KLDILTGGIL ETTGGNPGEL
     FRYVIADQFD RLRNGDRFWF ENTKTNLLNA SKISEILNTK FRDVIFRVNP TLNKSLDLQD
     NPFMWNTNGY KLFCPQPYQL NENVLEECTP LQRYDYFKSS EVSFPVSFAF FGVFVLVTIL
     FMHWLGHRRT KSAQNEKRKI TTNKRQATLV ASGNMTIATE VLGENVRQIQ IIFGPENTIQ
     TKLATRKKTL RTIELKRERK IEIINSNGTD RRTMIVRVEG ETYDLVLSFG DMSELDHFYN
     ELNTFLKSSR LHSEHHLIPE KHIMEDARTK EKRDEDLQQF FRAALSQAAN IRTDGDGINR
     HSVKELVNVT INKSELAEYL KLKEDSVFVE RMFTVADANE DGVVSFREFL DIIVLFTKGW
     ENEKAKMMFS MYDLDKSGGL SVSEFKTMLK SMIEIVESSP GSDQLDVDVE RMMQENGFSN
     KDSLTLDDFQ ILLGQCSSGG NGSAMHSGGL VCTPMARRMT RRVKTLRDDY KTKPHEKFLL
     ALVKLNQHYA NHIFCLALYC TITAGVFANA FFVVYSKNSS GLFGIGGSLM AIARASAAAL
     MFNFSTLLLT MCRNIITFLR ETFLHRYIPF DSAVTMHRII AWMAITFTAL HIVAHGINFY
     SIVTQSPDDM ACLFRDMWYP SDYVPTFVFW LFQTITGITG VILTLALIIM YVFASNYSRR
     LIFTWFRWTH KVGYMSLYFF TVLHGSGMLI IGFSPQFYYY FLVPAILFAL DKVYTYSRKK
     AYISVVRAEL YPSEVTHLEF KRPKNFDYKA GQWVRIACLA QSPTEYHPFT LSSAPHEDTL
     MLHIRAVGPW TRNLRKIYDP NVLRDSPYPK LYLDGPFGEG HQDWYKYEVS VLVGGGIGVT
     PFASILKDLI NRSQTGGGIT CKAVYFIWVT RDQKQYEWLT DIIQDVESKD AKQILNTHIF
     ITQFPQKFDL RTTMLYICEE NFQKISGKSL FTGLRAVTHF GRPDFTDFFA TLGEEHPSVE
     NFGVFSCGPA PMTKGVENAC SSLNKYTGPT YSHHFENF
//
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